KEGG ENZYME: 1.11.2.2

ENZYME: 1.11.2.2

Entry

EC 1.11.2.2 Enzyme

Name

myeloperoxidase;
MPO;
verdoperoxidase

Class

Oxidoreductases;
Acting on a peroxide as acceptor;
Peroxygenases

Sysname

chloride:hydrogen-peroxide oxidoreductase (hypochlorite-forming)

Reaction(IUBMB)

Cl- + H2O2 + H+ = HClO + H2O [RN:R09564]

Reaction(KEGG)

R09564;
(other) R11906

Substrate

Cl- [CPD:C00698];
H2O2 [CPD:C00027];
H+ [CPD:C00080]

Product

HClO [CPD:C19697];
H2O [CPD:C00001]

Comment

Contains calcium and covalently bound heme (proximal ligand histidine). It is present in phagosomes of neutrophils and monocytes, where the hypochlorite produced is strongly bactericidal. It differs from EC 1.11.1.10 chloride peroxidase in its preference for formation of hypochlorite over the chlorination of organic substrates under physiological conditions (pH 5-8). Hypochlorite in turn forms a number of antimicrobial products (Cl2, chloramines, hydroxyl radical, singlet oxygen). MPO also oxidizes bromide, iodide and thiocyanate. In the absence of halides, it oxidizes phenols and has a moderate peroxygenase activity toward styrene.

History

EC 1.11.2.2 created 2011

Pathway

ec00983

Drug metabolism - other enzymes

Orthology

K10789

myeloperoxidase

Genes

HSA:

4353(MPO)

PTR:	748680(MPO)

PPS:	100992079(MPO)

GGO:	101135280(MPO)

PON:	100461693(MPO)

NLE:	100606582(MPO)

MCC:	714246(MPO)

MCF:	102130410(MPO)

CSAB:

103242854(MPO)

RRO:	104669826(MPO)

RBB:	108521655(MPO)

CJC:	100408045(MPO)

SBQ:	101046117(MPO)

MMU:	17523(Mpo)

RNO:	303413(Mpo)

CGE:	100752227(Mpo) 100757792

NGI:	103741805(Mpo)

HGL:	101707361(Mpo)

CCAN:

109674413 109702951

OCU:	100340692(MPO)

TUP:	102501858(MPO)

CFA:	609986(MPO)

AML:	100472895(MPO)

UMR:	103667463(MPO)

ORO:	101380182(MPO)

FCA:	100142673(MPO)

PTG:	102973033(MPO)

AJU:	106989943(MPO)

BTA:	511206(MPO)

BOM:	102286491(MPO)

BIU:	109573426(MPO)

PHD:	102337926(MPO)

CHX:	102185772(MPO)

OAS:	101123053(MPO)

SSC:	100517120(MPO)

CFR:	102510136(MPO)

CDK:	105097806(MPO)

BACU:

103004965(MPO)

LVE:	103083642(MPO)

OOR:	101290133(MPO)

ECB:	100070920(MPO)

EPZ:	103546343(MPO)

EAI:	106822013(MPO)

MYB:	102240978(MPO)

MYD:	102756726(MPO)

HAI:	109379730(MPO)

RSS:	109449735(MPO)

PALE:

102883356(MPO)

LAV:	100662013(MPO)

TMU:

101340378

MDO:	100012330(MPO) 100022606

SHR:	100918289(MPO)

GGA:	417466(LPO) 417467(MPO)

MGP:	100547955(LPO)

APLA:

101801315 101805061

ACYG:

106041022 106041024(MPO)

TGU:	100228147(MPO)

GFR:	102037835(MPO)

FAB:	101820562(MPO)

CCW:

104695782

FPG:	101914689(MPO)

FCH:

102052208

CLV:	102084173 102084361

EGZ:	104131757 104131758(MPO)

NNI:	104012465(LPO)

ACUN:

113487144 113487180(MPO)

AAM:	106496096 106496104(MPO)

ASN:	102372031 102379880

AMJ:	102559230(LPO)

PSS:	102454048 102463089

CMY:	102933916 102934149 102941880(MPO)

CPIC:

101935994 101946833 101947097(MPO)

ACS:	100567371 103282013 107983822

PVT:	110084498 110084515

PBI:	103057971 103062626

PMUR:

107288569 107288571(MPO)

GJA:

107112485

XLA:	373710(mpo.S) 394386(mpo.L) 398084(epx.L)

XTR:	100490938(mpo) 100496213(epx)

NPR:	108785838 108785844 108797850

SRX:

SANH:

SGH:

CCAR:

SASA:

100380666(perm) 106572735 106572795

OTW:

112231092

SALP:

111964113

SFM:

108932527

LCM:	102347787 102348047(MPO)

» show all

Reference

Authors

Agner, K.

Title

Myeloperoxidase.

Journal

Adv Enzymol 3:137-148 (1943)

Reference

2 [PMID:176150]

Authors

Harrison JE, Schultz J

Title

Studies on the chlorinating activity of myeloperoxidase.

Journal

J Biol Chem 251:1371-4 (1976)

Reference

3 [PMID:9922160]

Authors

Furtmuller PG, Burner U, Obinger C

Title

Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate.

Journal

Biochemistry 37:17923-30 (1998)

Reference

4 [PMID:10652281]

Authors

Tuynman A, Spelberg JL, Kooter IM, Schoemaker HE, Wever R

Title

Enantioselective epoxidation and carbon-carbon bond cleavage catalyzed by Coprinus cinereus peroxidase and myeloperoxidase.

Journal

J Biol Chem 275:3025-30 (2000)
DOI:10.1074/jbc.275.5.3025

Reference

5 [PMID:15689384]

Authors

Klebanoff SJ

Title

Myeloperoxidase: friend and foe.

Journal

J Leukoc Biol 77:598-625 (2005)
DOI:10.1189/jlb.1204697

Reference

6 [PMID:10766826]

Authors

Fiedler TJ, Davey CA, Fenna RE

Title

X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.

Journal

J Biol Chem 275:11964-71 (2000)
DOI:10.1074/jbc.275.16.11964

Sequence

[hsa:4353]

Reference

7 [PMID:11593004]

Authors

Gaut JP, Yeh GC, Tran HD, Byun J, Henderson JP, Richter GM, Brennan ML, Lusis AJ, Belaaouaj A, Hotchkiss RS, Heinecke JW

Title

Neutrophils employ the myeloperoxidase system to generate antimicrobial brominating and chlorinating oxidants during sepsis.

Journal

Proc Natl Acad Sci U S A 98:11961-6 (2001)
DOI:10.1073/pnas.211190298

Other DBs

ExplorEnz - The Enzyme Database:

1.11.2.2

IUBMB Enzyme Nomenclature:

1.11.2.2

ExPASy - ENZYME nomenclature database:

1.11.2.2

BRENDA, the Enzyme Database:

1.11.2.2

DBGET integrated database retrieval system